Molecular Dynamics Studies of Protein and Peptide Folding and Unfolding
Proteins are fascinating. As objects in three-dimensional space, they are sometimes elegant and always complex molecules, yet they consist of only 20 different amino acid building blocks. The function of proteins is determined by their three-dimensional structure, and the majority of biological processes involve one or more protein molecules. The mechanism of the evolutionary development of specific proteins is one of the unsolved problems of biology. Most proteins are very sensitive to their environment; small temperature or pH changes can alter both their stability and their ability to function. The native structure of a protein is determined by the amino acid sequence (Anfinsen, 1972). In solution, many proteins have been shown to refold by themselves under conditions that lead to a stable native state, but in vivo the folding process can be very complicated and often involves other proteins, such as chaperones (Gething and Sambrook, 1992).
KeywordsMolecular Dynamic Simulation Root Mean Square Root Mean Square Deviation Hydrophobic Core Bovine Pancreatic Trypsin Inhibitor
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- Dobson CM, Hanley C, Radford SE, Baum JA, Evans PA (1991): In Conformations and Forces in Protein Folding. Nall BT, Dill KA, eds. pages 175-181Google Scholar
- Karle IL, Flippen-Anderson JL, Uma K, Balaram P (1990): Apolar peptide models for conformational heterogeneity, hydration, and packing of Polypeptide helices: Crystal structure of hepta-and octapeptides containing α-aminoisobutyric acid. Proteins: Structure, Function and Genetics 7:62–73CrossRefGoogle Scholar
- Karplus M, Shakhnovich E (1992): Protein folding: Theoretical studies of thermodynamics and dynamics. In Protein Folding. Creighton TE, ed. New York: WH FreemanGoogle Scholar
- Levinthal C (1969): In Mössbauer Spectroscopy in Biological Systems, DeGennes P et al., eds. Urbana, IL: University of Illinois Press. Proceedings of a meeting held at Allerton House, Monticello, ILGoogle Scholar
- Ptitsyn OB (1992): The molten globule state. In Protein Folding, Creighton TE, ed. New York: WH Freeman, pages 243–300Google Scholar